Current techniques of pulse Fourier transform and correlation proton and carbon-13 nuclear resonance spectroscopy will be used to investigate certain problems in protein chemistry. Nmr peaks corresponding to residues of interest will be resolved and assigned by means of carbon-13 and deuterium isotopic substitutions. Information concerning the chemical environments, protonation states and mobilities of individual protein groups will be derived from the nmr data. This information will be used to follow conformational transitions and microscopic proton dissociation steps in the proteins. The problems under investigation include: (1) comparative studies of the active sites of serine proteases, (2) the mechanisms of interactions between protein proteinase inhibitors and proteinases, (3) the structures of glycoproteins, (4) and mechanisms of protein folding.